MolNFT v1 · #58790 · protein

Crystal structure of cryptosporidium parvum adenylate kinase CGD5_3360

3BE4: “Crystal structure of cryptosporidium parvum adenylate kinase CGD5_3360”. X-ray diffraction, 2 ligands (AP5, MG), 1 pocket (best druggability 0.81). MolNFT v1 #58790 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3BE4
Type: protein
Length: 215 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylate kinase
UniProt: Q5CRC5
Ligands: AP5, MG
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenylate kinase	protein	215	49% helix, 16% strand	Q5CRC5

Ligands and binding sites

AP5 · Bis(adenosine)-5'-pentaphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
GOL · Glycerol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	659	0.81	0.85	83	MG, AP5, GOL

Compared structures

3BE4 · Crystal structure of Cryptosporidium parvum adenylate kinase cgd5_3360 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5CRC5
Elsewhere: RCSB PDB 3BE4 · PDBe 3BE4 · UniProt Q5CRC5

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